Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins. - Wikidata - awgldk - TriplyDB

Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins.

Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins.

http://www.wikidata.org/entity/Q34372400

about

Metabolism leaves its mark on the powerhouse: recent progress in post-translational modifications of lysine in mitochondria Regulation of G6PD acetylation by SIRT2 and KAT9 modulates NADPH homeostasis and cell survival during oxidative stress Sirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex activity Effects of Oxidative Stress on Mesenchymal Stem Cell Biology Emerging therapeutic roles for NAD(+) metabolism in mitochondrial and age-related disorders Interdependence of nutrient metabolism and the circadian clock system: Importance for metabolic health Potential Modulation of Sirtuins by Oxidative Stress Chemical reporters for exploring protein acylation SIRT3 regulates progression and development of diseases of aging.Interplay between sirtuins, MYC and hypoxia-inducible factor in cancer-associated metabolic reprogramming Sirtuins, metabolism, and DNA repair Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases Sirtuins in epigenetic regulation Chemical probing of the human sirtuin 5 active site reveals its substrate acyl specificity and peptide-based inhibitors Structure-Based Development of an Affinity Probe for Sirtuin 2 Undercover: gene control by metabolites and metabolic enzymes The role of sirtuins in cellular homeostasis Coupling circadian rhythms of metabolism and chromatin remodelling Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens Slowing ageing by design: the rise of NAD(+) and sirtuin-activating compounds Synthesis and Assay of SIRT1-Activating Compounds Structural Basis of Sirtuin 6 Activation by Synthetic Small Molecules.A continuous sirtuin activity assay without any coupling to enzymatic or chemical reactions.Selective Sirt2 inhibition by ligand-induced rearrangement of the active site.Role of the Substrate Specificity-Defining Residues of Human SIRT5 in Modulating the Structural Stability and Inhibitory Features of the Enzyme.Insights into Lysine Deacetylation of Natively Folded Substrate Proteins by Sirtuins.Fatty acylation of proteins: The long and the short of it.SIRT6 interacts with TRF2 and promotes its degradation in response to DNA damage.Partitioning circadian transcription by SIRT6 leads to segregated control of cellular metabolism.A Chemical Biology Approach to Reveal Sirt6-targeted Histone H3 Sites in Nucleosomes.Sirtuins: guardians of mammalian healthspan.The Identification of a SIRT6 Activator from Brown Algae Fucus distichus Interplay between epigenetics and metabolism in oncogenesis: mechanisms and therapeutic approaches Role of NAD+ and mitochondrial sirtuins in cardiac and renal diseases It takes two to tango: NAD+ and sirtuins in aging/longevity control Thiomyristoyl peptides as cell-permeable Sirt6 inhibitors.Metabolic reprogramming and dysregulated metabolism: cause, consequence and/or enabler of environmental carcinogenesis?Global profiling of protein lipidation using chemical proteomic technologies Posttranslational modification of Sirt6 activity by peroxynitrite.Identification of 'erasers' for lysine crotonylated histone marks using a chemical proteomics approach.

P2860

Q21129226-B301667F-C081-4B68-A26A-0E8E56D3E4CB Q24295960-AC234D11-DACB-4619-A873-EE1AF2D02939 Q24310540-85D221F6-2892-4EF2-AECE-3A3AB38665B1 Q26740408-013B29D8-16BC-4A7E-B0CB-A335DC7171D9 Q26741300-3CCEDC2D-24DC-452E-BD7D-8558C73F6174 Q26765492-59F3DF72-A7C4-4888-B6A1-201A479C3780 Q26770803-07D0647C-40DF-474D-A471-BE9DC919E25E Q26849219-C00E87DD-A9FC-4A5A-BA97-F79AD7AD5813 Q26864656-C4D171CD-5552-4817-98D7-C7194B40D233 Q26991931-70F64CB6-C5E1-494B-8AD7-BEADDEBE2B23 Q27015759-3689BE74-D67A-4B6E-941C-00533B20DA70 Q27024524-55C1939E-798E-4046-A02D-C3CF6726E984 Q27026861-AECFB700-DA0E-4F90-A5EC-6B2EB59C01E2 Q27694761-58329D9E-3793-4ED2-9D5A-1E0B1163D247 Q27703530-AE523EBC-8C24-4F54-B40C-3762FE95AE4F Q28072281-C1E2D9DC-B122-403F-9008-22B7506207E9 Q28075581-1350C30C-1E5C-4CF4-9027-9525C0C3E667 Q28080676-49ED0B44-46DC-47E5-9140-535687855E2B Q28264979-035A939D-69E2-4EB4-8890-CB139481BF72 Q28314993-8CF13AFD-C98C-4742-B5E7-5379A1BC20EF Q28818352-96545FA6-571F-4480-8C4E-75AD64106EE3 Q30313597-236481C2-781D-4656-BA45-01480968C2B5 Q30315509-37152E4C-A23A-45A0-9A6E-A1B27FEB9555 Q30316777-2DF9A702-3637-45CF-8C80-5B14DF91E077 Q30386186-2AC62223-D8F4-4ACF-AA68-61DA5B62F2EF Q30388525-57EB0475-4519-4D8D-AAD7-FCFEE761A7F3 Q30388573-8C1166FE-22D1-40F1-8F36-964747E092A2 Q33558275-95D37542-4F40-4753-9267-6F650D7D2C34 Q33803483-24360352-7A47-4E4E-837D-16060C1BCDDD Q33817548-87A5951E-9EE9-4876-A0C7-396A289DF936 Q33831420-2799A0B1-38A5-49AA-96F8-2C7666806A2A Q33833447-29F72529-B547-4A01-A4A5-DF013B095D9C Q33835913-1115B7E8-8159-460F-A01E-B986E0F13C9C Q33899993-A16E8094-3CEA-49EB-B567-F1A1AD4F91EE Q33914309-E69D6348-383C-4620-905A-DB6E844C8747 Q34167531-B9D963DD-28E7-4DA1-BF64-6872C0FD7174 Q34482056-760CCD88-889A-4DA9-8465-E0B863A9B408 Q35057612-934816F4-613B-4241-A8AE-DB82E6B993D9 Q35118010-F3D8B073-F09E-419A-9174-BF25B42BB522 Q35173191-21BA761F-CA3B-4344-9256-8253EB19D2EE

P2860

Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins.

http://www.wikidata.org/entity/Q34372400

description

2013 nî lūn-bûn

@nan

2013 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

Activation of the protein deac ...... ylation by mammalian sirtuins.

@ast

Activation of the protein deac ...... ylation by mammalian sirtuins.

@en

Activation of the protein deac ...... ylation by mammalian sirtuins.

@nl

type

label

Activation of the protein deac ...... ylation by mammalian sirtuins.

@ast

Activation of the protein deac ...... ylation by mammalian sirtuins.

@en

Activation of the protein deac ...... ylation by mammalian sirtuins.

@nl

prefLabel

Activation of the protein deac ...... ylation by mammalian sirtuins.

@ast

Activation of the protein deac ...... ylation by mammalian sirtuins.

@en

Activation of the protein deac ...... ylation by mammalian sirtuins.

@nl

P1433

Q34372400-037D9D73-F7B9-4C90-812E-616D5D49691B

P1476

Q34372400-8BAF5815-A78D-415D-8AD6-21C2A3AF64AF

P2093

Q34372400-9190CB71-F61F-4342-B821-9E171DC78DDD

Q34372400-D71FE502-384A-4B6F-A47B-092BE0B15195

P2860

Q34372400-01823E23-8E95-4C05-8857-D5FCD2C8A227

Q34372400-04207EE4-C30B-41A7-87DC-C4D3E05D1937

Q34372400-147A7BDB-2514-4366-A0AB-2C60899CA4A6

Q34372400-14D116AA-0C7E-4C6E-9891-8AFB8F207CDE

Q34372400-21E64ABD-FD49-456E-A0EC-199536513D10

Q34372400-28215475-600F-489B-A92F-8683C673D5EA

Q34372400-304D7F47-483A-4EC3-8824-4051C501317D

Q34372400-3103E736-A272-40EE-A14F-AE29FBAC5948

Q34372400-3A6D9737-ACFF-4C94-A59F-D0D41E2C284B

Q34372400-3B1FF198-4B8F-4BDB-822E-87F3D00A44DD

P304

Q34372400-0735A0C6-69DF-4975-BB0D-1B47FD6A48BF

P31

Q34372400-44D0C264-FAEE-4729-A367-DEA9431AC2CB

P356

Q34372400-CC30A8A9-CEBD-484B-BECE-80BD58ADC1B6

P407

Q34372400-774A9BD7-1EDB-4058-9A3F-B336F9C7D1E7

P433

Q34372400-76CCB2BC-C72D-49B8-A48A-3023C475B268

P478

Q34372400-211B625A-5AF2-490F-8463-0D92152AF56E

P50

Q34372400-10968620-27D0-40CB-A81F-3DD5D59CE94E

P577

Q34372400-177EF0BB-648E-429F-B852-568219409855

P698

Q34372400-1E70BC35-F175-443E-8A9B-2E55FC0F5C86

P921

Q34372400-195BD20D-438C-4073-AF6E-243BF7938D99

P932

Q34372400-60C0BDF7-EBBD-45D3-A8BE-3110657DE1A1

P356

JBC.C113.511261

P1433

Journal of Biological Chemistry

P1476

Activation of the protein deac ...... ylation by mammalian sirtuins.

@en

P2093

Jessica L Feldman

http://www.w3.org/2001/XMLSchema#string

John M Denu

http://www.w3.org/2001/XMLSchema#string

P2860

Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase

Human SIRT6 promotes DNA end resection through CtIP deacetylation

The histone deacetylase SIRT6 is a tumor suppressor that controls cancer metabolism

SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin

SIRT6 links histone H3 lysine 9 deacetylation to NF-kappaB-dependent gene expression and organismal life span

Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine

Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification

Protein lysine acylation and cysteine succination by intermediates of energy metabolism

Plasmodium falciparum Sir2A Preferentially Hydrolyzes Medium and Long Chain Fatty Acyl Lysine

P304

31350-31356

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.C113.511261

http://www.w3.org/2001/XMLSchema#string

P407

P433

43

http://www.w3.org/2001/XMLSchema#string

P478

288

http://www.w3.org/2001/XMLSchema#string

P50

P577

2013-09-18T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

24052263

http://www.w3.org/2001/XMLSchema#string

P921

P932

3829447

http://www.w3.org/2001/XMLSchema#string